BMRB Entry 30155

Name: NMR solution structure of the RRM1 domain of the post-transcriptional regulator HuR
Published: 2017-08-04

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PDB ID: 5szw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30155
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR solution structure of the RRM1 domain of the post-transcriptional regulator HuR

Deposition date:

2016-08-15

Original release date:

2017-08-04

Authors:

Lixa, C.; Mujo, A.; Jendiroba, K.; Almeida, F.; Lima, L.; Pinheiro, A.

Citation:

Citation: Lixa, C.; Mujo, A.; Magalhaes, M.; Almeida, F.; Lima, L.; Pinheiro, A.. "Oligomeric transition and dynamics of RNA binding by the HuR RRM1 domain in solution" J. Biomol. NMR 72, 179-192 (2018).
PubMed: 30535889

Assembly members:

Assembly members:
entity_1, polymer, 101 residues, 11220.585 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMSNGYEDHMAEDCRGDIG RTNLIVNYLPQNMTQDELRS LFSSIGEVESAKLIRDKVAG HSLGYGFVNYVTAKDAERAI NTLNGLRLQSKTIKVSYARP S

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	412
15N chemical shifts	106
1H chemical shifts	666

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 101 residues - 11220.585 Da.

1

GLY

HIS

MET

SER

ASN

GLY

TYR

GLU

ASP

HIS

2

MET

ALA

GLU

ASP

CYS

ARG

GLY

ASP

ILE

GLY

3

ARG

THR

ASN

LEU

ILE

VAL

ASN

TYR

LEU

PRO

4

GLN

ASN

MET

THR

GLN

ASP

GLU

LEU

ARG

SER

5

LEU

PHE

SER

ILE

GLY

GLU

VAL

GLU

SER

6

ALA

LYS

LEU

ILE

ARG

ASP

LYS

VAL

ALA

GLY

7

HIS

SER

LEU

GLY

TYR

GLY

PHE

VAL

ASN

TYR

8

VAL

THR

ALA

LYS

ASP

ALA

GLU

ARG

ALA

ILE

9

ASN

THR

LEU

ASN

GLY

LEU

ARG

LEU

GLN

SER

10

LYS

THR

ILE

LYS

VAL

SER

TYR

ALA

ARG

PRO

11

SER

Samples:

sample_1: DTT 10 mM; HuR_RRM1, [U-15N], 1.5 mM; sodium chloride 100 mM; sodium phosphate 30 mM

sample_2: DTT 10 mM; HuR_RRM1, [U-100% 13C; U-100% 15N], 1.5 mM; sodium chloride 100 mM; sodium phosphate 30 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HC(C)H-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

CcpNMR, CCPN - data analysis

TOPSPIN v3.1, Bruker Biospin - processing

NMR spectrometers:

Bruker DRX 600 MHz
Bruker AvanceIII 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks